Cargando…

Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades

PURPOSE: Advanced glycation end products of BSA (AGE-BSA) participate in the pathogenesis of diabetic vascular disease. However, the role of AGE-BSA in diabetic retinopathy, especially in retinal neovascularization, remains incomplete. This study aimed to determine the contributions of AGE-BSA in th...

Descripción completa

Detalles Bibliográficos
Autores principales: Ma, Jianli, Liu, Ting, Dong, Xiaoguang
Formato: Texto
Lenguaje:English
Publicado: Molecular Vision 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3002957/
https://www.ncbi.nlm.nih.gov/pubmed/21179235
_version_ 1782193813410807808
author Ma, Jianli
Liu, Ting
Dong, Xiaoguang
author_facet Ma, Jianli
Liu, Ting
Dong, Xiaoguang
author_sort Ma, Jianli
collection PubMed
description PURPOSE: Advanced glycation end products of BSA (AGE-BSA) participate in the pathogenesis of diabetic vascular disease. However, the role of AGE-BSA in diabetic retinopathy, especially in retinal neovascularization, remains incomplete. This study aimed to determine the contributions of AGE-BSA in the endothelial-to-mesenchymal transition (EnMT) of cultured human and monkey endothelial cell lines and the mechanism that may be related with the transition. METHODS: Monkey choroid-retinal endothelial cells (RF/6A) and human umbilical vein endothelial cells (HUVEC) were cultured in Dulbecco’s modified Eagle’s Medium (DMEM) and Ham’s F12 medium containing 200 mg/l AGE-BSA. The expression of VE-cadherin, β-catenin, vimentin, N-cadherin, and protein kinase B (AKT2) was observed by immunocytochemistry and flow cytometry. Cell motility was determined by migration assays; the endothelial function of the formatting tube was measured by tube formation assays, while the change in the polarity was measured using resistance instruments. RESULTS: The characteristics of EnMT included loss of endothelial markers of VE-cadherin and β-catenin, which were replaced by mesenchymal markers of vimentin and N-cadherin, enhanced migration and tube formation, and diminished polarity. AGE-BSA contributed to upregulation of the protein expression of VE-cadherin and β-catenin and downregulation of protein expression of vimentin and N-cadherin, leading to enhanced migration and tube formation and diminished polarity. During this process, expression of AKT2 was upregulated. CONCLUSIONS: AGE-BSA can induce EnMT of cultured human and monkey endothelial cells. The signal pathway involving AKT2 may play a role in this process.
format Text
id pubmed-3002957
institution National Center for Biotechnology Information
language English
publishDate 2010
publisher Molecular Vision
record_format MEDLINE/PubMed
spelling pubmed-30029572010-12-22 Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades Ma, Jianli Liu, Ting Dong, Xiaoguang Mol Vis Research Article PURPOSE: Advanced glycation end products of BSA (AGE-BSA) participate in the pathogenesis of diabetic vascular disease. However, the role of AGE-BSA in diabetic retinopathy, especially in retinal neovascularization, remains incomplete. This study aimed to determine the contributions of AGE-BSA in the endothelial-to-mesenchymal transition (EnMT) of cultured human and monkey endothelial cell lines and the mechanism that may be related with the transition. METHODS: Monkey choroid-retinal endothelial cells (RF/6A) and human umbilical vein endothelial cells (HUVEC) were cultured in Dulbecco’s modified Eagle’s Medium (DMEM) and Ham’s F12 medium containing 200 mg/l AGE-BSA. The expression of VE-cadherin, β-catenin, vimentin, N-cadherin, and protein kinase B (AKT2) was observed by immunocytochemistry and flow cytometry. Cell motility was determined by migration assays; the endothelial function of the formatting tube was measured by tube formation assays, while the change in the polarity was measured using resistance instruments. RESULTS: The characteristics of EnMT included loss of endothelial markers of VE-cadherin and β-catenin, which were replaced by mesenchymal markers of vimentin and N-cadherin, enhanced migration and tube formation, and diminished polarity. AGE-BSA contributed to upregulation of the protein expression of VE-cadherin and β-catenin and downregulation of protein expression of vimentin and N-cadherin, leading to enhanced migration and tube formation and diminished polarity. During this process, expression of AKT2 was upregulated. CONCLUSIONS: AGE-BSA can induce EnMT of cultured human and monkey endothelial cells. The signal pathway involving AKT2 may play a role in this process. Molecular Vision 2010-12-09 /pmc/articles/PMC3002957/ /pubmed/21179235 Text en Copyright © 2010 Molecular Vision. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Ma, Jianli
Liu, Ting
Dong, Xiaoguang
Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades
title Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades
title_full Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades
title_fullStr Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades
title_full_unstemmed Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades
title_short Advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase B signaling cascades
title_sort advanced glycation end products of bovine serum albumin-induced endothelial-to-mesenchymal transition in cultured human and monkey endothelial cells via protein kinase b signaling cascades
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3002957/
https://www.ncbi.nlm.nih.gov/pubmed/21179235
work_keys_str_mv AT majianli advancedglycationendproductsofbovineserumalbumininducedendothelialtomesenchymaltransitioninculturedhumanandmonkeyendothelialcellsviaproteinkinasebsignalingcascades
AT liuting advancedglycationendproductsofbovineserumalbumininducedendothelialtomesenchymaltransitioninculturedhumanandmonkeyendothelialcellsviaproteinkinasebsignalingcascades
AT dongxiaoguang advancedglycationendproductsofbovineserumalbumininducedendothelialtomesenchymaltransitioninculturedhumanandmonkeyendothelialcellsviaproteinkinasebsignalingcascades